ID A0A199V661_ANACO Unreviewed; 673 AA.
AC A0A199V661;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative L-type lectin-domain containing receptor kinase S.5 {ECO:0000313|EMBL:OAY72376.1};
GN ORFNames=ACMD2_26124 {ECO:0000313|EMBL:OAY72376.1};
OS Ananas comosus (Pineapple) (Ananas ananas).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Bromeliaceae;
OC Bromelioideae; Ananas.
OX NCBI_TaxID=4615 {ECO:0000313|EMBL:OAY72376.1, ECO:0000313|Proteomes:UP000092600};
RN [1] {ECO:0000313|EMBL:OAY72376.1, ECO:0000313|Proteomes:UP000092600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MD2 {ECO:0000313|Proteomes:UP000092600};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY72376.1};
RX PubMed=27374615; DOI=10.1093/dnares/dsw026;
RA Redwan R.M., Saidin A., Kumar S.V.;
RT "The draft genome of MD-2 pineapple using hybrid error correction of long
RT reads.";
RL DNA Res. 0:0-0(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC superfamily. Ser/Thr protein kinase family.
CC {ECO:0000256|ARBA:ARBA00010217}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the leguminous lectin
CC family. {ECO:0000256|ARBA:ARBA00008536}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAY72376.1}.
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DR EMBL; LSRQ01003122; OAY72376.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A199V661; -.
DR STRING; 4615.A0A199V661; -.
DR Proteomes; UP000092600; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0098542; P:defense response to other organism; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001220; Legume_lectin_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR27007; -; 1.
DR PANTHER; PTHR27007:SF48; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00139; Lectin_legB; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OAY72376.1};
KW Lectin {ECO:0000256|ARBA:ARBA00022734, ECO:0000313|EMBL:OAY72376.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:OAY72376.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000092600};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..673
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008508264"
FT TRANSMEM 263..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 326..613
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 106..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 673 AA; 73503 MW; 5EF6D767B65D5EB6 CRC64;
MGGAGRSLLR HLPTAAAAAL FLLLLLAPTA HSQSTPKENV TFSFSSFDDS FRSTNLTVNG
DSSIAQGALQ ITPDTLNQAS YLVNRSGRVL YSQPFKLWEY TPANVSGSSS SSSSNNGNGS
SNSNSNSNKY VASFSTSFTI NLDTVKQPYD PDDNHVGLDV NGVVSVANAS LDLQIAPVAP
ANYTLWIDYD GGVRRIRVYM AAEGRPQPPS PVLDAPLDLG QFVLQRSYFG FSASTGSDYE
LNCVLAWNMT VERLRDKKRL PRWALGLAVG LPCAALLLGL IAGLYYVRRR RVGDDPSMLA
GALLRSLPGT PREFDYKELK KATNNFDEKM KLGQGGFGTV YEGVLVGAGD NGETIEVAVK
KFARANTKGQ EEFLAELTII NRLRHRHLVR LIGWCHQNGE LLLVYDYMPE GSLDQHLFGG
PEKPLLNWAR RYNVLSGVAS ALHYLHNEYD QRVVHRDLKA SNVMLDRDFN ARLGDFGLAR
ALDVDRTSYA DLELDGVPGT LGYIAPECFH TGKATRESDV YGFGAVILEV VCGLRPRCEV
GGFHYLVDWV WKLYREGRIL EAVDVRLAGD FVGADAERLL LLGLACSHPI PGERPKTQDI
MQILLRSMQP PAVPPFKPAF VWPSAVPDGD GETTTTTTAS GLTGSSYYAS SAGWTSNYVS
RDGHVSEDDV PMV
//
